Hejun Liu, M. Yuan, Deli Huang, S. Bangaru, C. D. Lee, Linghang Peng, Xueyong Zhu, D. Nemazee, M. V. van Gils, R. Sanders, H. Kornau, S. Reincke, H. Prüss, Jakob Kreye, N. Wu, A. Ward, I. Wilson
bioRxiv : the preprint server for biology, 2021
Coronaviruses have caused several epidemics and pandemics including the ongoing coronavirus disease 2019 (COVID-19). Some prophylactic vaccines and therapeutic antibodies have already showed striking effectiveness against COVID-19. Nevertheless, concerns remain about antigenic drift in SARS-CoV-2 as well as threats from other sarbecoviruses. Cross-neutralizing antibodies to SARS-related viruses provide opportunities to address such concerns. Here, we report on crystal structures of a cross-neutralizing antibody CV38-142 in complex with the receptor binding domains from SARS-CoV-2 and SARS-CoV. Our structural findings provide mechanistic insights into how this antibody can accommodate antigenic variation in these viruses. CV38-142 synergizes with other cross-neutralizing antibodies, in particular COVA1-16, to enhance neutralization of SARS-CoV-2 and SARS-CoV. Overall, this study provides valuable information for vaccine and therapeutic design to address current and future antigenic drift in SARS-CoV-2 and to protect against zoonotic coronaviruses.
Cited by 10 publications.
Field of study: Biology